Introduction
ASFV has a 170–194 kb double-stranded DNA genome that contains over 150 open reading frames (ORFs), encoding at least 68 structural proteins, most of which have unknown functions. ASFV particles have a complex multi-envelope structure that includes the nucleoid, core shell, inner envelope, icosahedral capsid, and outer envelope. Interestingly, one glycoprotein in the outer envelope of the virus, CD2v, encoded by the EP402R gene, is a homolog of the T cell adhesion molecule CD2. CD2v has a signal peptide, two extracellular immunoglobulin-like domains, a transmembrane (TM) region, and an intracellular region (referred to as CD2v-IR) that contains an acidic domain and proline-rich repetitive sequences. This proline-rich region has been reported to interact with the mammalian actin-binding protein 1 (mAbp1), and this may control protein transport involved in immune regulation. The CD2v-IR domain binds the trans-Golgi network (TGN) protein complex AP-1, affecting virus infectivity.
COA
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